Purification, characterization, and expression of AP025 protease from Thermoascus aurantiacus.

Janine Lin, Wenping Wu, Jan Lehmbeck, and Debbie Yaver.

Author address: 

Novozymes Biotech, Inc, Davis CA.


A metalloprotease AP025 was purified from culture broth of a thermophilic fungus Thermoascus aurantiacus. The AP025 protease has high optimal temperature (70778;C), and is most active at low pH (pH 6). The enzyme is most stable at pH 4, but is also stable from pH 4-10. The AP025 protease may have potential in industrial applications. The gene encoding the protease AP25 was cloned and sequence analysis showed that this protease is a metalloprotease. The cDNA of the AP025 gene was successfully expressed under two variants of Aspergillus niger amylase promoter in Aspergillus oryzae and in Fusarium venenatum under the control of the F. venenatum glucoamylase promoter. Expression of AP025 under a stronger promoter in A. oryzae resulted in the highest yield of AP025.

abstract No: 


Full conference title: 

23rd Fungal Genetics Conference
    • Fungal Genetics Conference 23rd (2002)